ZEB1_CHICK
ID ZEB1_CHICK Reviewed; 1114 AA.
AC P36197; O42408;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Zinc finger E-box-binding homeobox 1;
DE AltName: Full=Delta EF1;
DE AltName: Full=Delta-crystallin enhancer-binding factor;
DE AltName: Full=Transcription factor 8;
DE Short=TCF-8;
GN Name=ZEB1; Synonyms=TCF8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=7904558; DOI=10.1242/dev.119.2.433;
RA Funahashi J., Sekido R., Murai K., Kamachi Y., Kondoh H.;
RT "Delta-crystallin enhancer binding protein delta EF1 is a zinc finger-
RT homeodomain protein implicated in postgastrulation embryogenesis.";
RL Development 119:433-446(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Embryo;
RX PubMed=8964504; DOI=10.1016/0378-1119(96)00185-0;
RA Sekido R., Takagi T., Okanami M., Moribe H., Yamamura M., Higashi Y.,
RA Kondoh H.;
RT "Organization of the gene encoding transcriptional repressor deltaEF1 and
RT cross-species conservation of its domains.";
RL Gene 173:227-232(1996).
CC -!- FUNCTION: Acts as a transcriptional repressor. Positively regulates
CC neuronal differentiation. Represses transcription by binding to the E
CC box-containing promoter (By similarity). Binds to delta 1-crystallin
CC enhancer core and represses lens-specific transcription. It binds as
CC well many other non-lens specific DNA sequences. {ECO:0000250}.
CC -!- SUBUNIT: May interact with CTBP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expression is developmentally regulated with high
CC expression in mesoderm, nervous system and lens.
CC -!- DEVELOPMENTAL STAGE: Expression starts after gastrulation, when
CC organogenesis has just begun.
CC -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC family. {ECO:0000305}.
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DR EMBL; D14313; BAA03259.1; -; mRNA.
DR EMBL; D76434; BAA11178.1; -; Genomic_DNA.
DR PIR; I50222; I50222.
DR RefSeq; NP_990462.1; NM_205131.1.
DR AlphaFoldDB; P36197; -.
DR BMRB; P36197; -.
DR STRING; 9031.ENSGALP00000011738; -.
DR PaxDb; P36197; -.
DR GeneID; 396029; -.
DR KEGG; gga:396029; -.
DR CTD; 6935; -.
DR VEuPathDB; HostDB:geneid_396029; -.
DR eggNOG; KOG3623; Eukaryota.
DR InParanoid; P36197; -.
DR OrthoDB; 890458at2759; -.
DR PhylomeDB; P36197; -.
DR PRO; PR:P36197; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR Pfam; PF05605; zf-Di19; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW DNA-binding; Homeobox; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1114
FT /note="Zinc finger E-box-binding homeobox 1"
FT /id="PRO_0000047235"
FT ZN_FING 170..193
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 240..262
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..292
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 581..640
FT /note="Homeobox; atypical"
FT ZN_FING 904..926
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 932..954
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 960..981
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 767..771
FT /note="CTBP-binding motif"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1050
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1080
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 299
FT /note="K -> N (in Ref. 2; BAA11178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1114 AA; 123151 MW; D914284143E7D279 CRC64;
MADGPRCKRR KQANPRRNNV TNYNNVIEAN SDSDDEDKLH IVEEESITDA ADCDASVPED
DLPTDHTVLP ENSEREGSTN SCWEDEGKET KEILGPEAQS DEVGCTVKED ECDSDAENEQ
NHDPNVEEFL QQEDTAVIYP EAPEEDQRQG TPEASGQDEN GTPDAFSQLL TCPYCDRGYK
RFTSLKEHIK YRHEKNEDNF SCSLCSYTFA YRTQLDRHMT SHKSGRDQRH VTQSSGNRKF
KCTECGKAFK YKHHLKEHLR IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCIGLMPVKG
RARSGLKTSQ CSSPSLSASP GSPARPQIRQ KIENKPLQEQ LPVNQIKTEP VDYEFKPIVV
ASGINCSTPL QNGVFSGGSP LQATSSPQGV VQAVVLPTVG LVSPISINLS DIQNVLKVAV
DGNVIRQVLE NNHANLASKE QETISNASIQ QAGHSLISAI SLPLVDQDGT TKIIINYSLE
QPSQLQVVPQ NLKKEHSVPT NSCKNEKLPE DLTVKSEKDK NFEGETNDST CLLCDDCPGD
LNALQELKHY ETKNPPQLPQ SSGTEAEKPS SPAPSETGEN NLSPGQPPLK NLLSLLKAYY
ALNAQPSAEE LSKIADSVNL PLDVVKKWFE KMQAGQISVQ SSGPSSPEQV KISSPTDNDD
QAATTNESEP QNSTNNSQNP ANTSKSQTSS GGSTQNGSRS STPSPSPLNL SSSRNSQGYT
YTAEGVQEEP QMEPLDLSLP KQHGELLERS TITSVYQNSV YSVQEEPLNL TCAKKEPQKD
NSITDSDPIV NVIPPSANPI NIAIPTVTAQ LPTIVAIADQ NSVPCLRALA ANKQTILIPQ
VAYTYSTTVS PAVQETPPKQ TQANGSQDER QDTSSEGVSN VEDQNDSDST PPKKKMRKTE
NGMYACDLCD KIFQKSSSLL RHKYEHTGKR PHECGICKKA FKHKHHLIEH MRLHSGEKPY
QCDKCGKRFS HSGSYSQHMN HRYSYCKREA EERDSTEQEE VGQEVLSSEH AGARASPSQI
DSDERESLTR EEEEDSEKEE EEEEEKDVEG LQEEKECRKL QDVEEEEEVE EEEEEEEGKT
EGNKNDDVVN RASNAEPEVI QSNGQVSEEK TNKA
